Ser402

Site Information
GLQLPFSsWYVDRGG SwissProt Entrez-Gene
Blast this site against: NCBI SwissProt PDB
Site Group ID: 25792201

In vivo Characterization
Methods used to characterize site in vivo:	immunoprecipitation ( 5 ) , mass spectrometry ( 5 ) , mutation of modification site ( 1 , 2 , 3 , 4 , 5 ) , western blotting ( 1 , 2 , 4 , 5 )
Disease tissue studied:	Parkinson's disease ( 3 )
Relevant cell line - cell type - tissue:	293 (epithelial) ( 5 ) , COS (fibroblast) ( 2 ) , HEK293T (epithelial) ( 2 ) , HeLa (cervical) ( 1 , 2 , 3 , 5 ) , MEF (fibroblast) ( 2 , 4 )

Downstream Regulation
Effects of modification on PINK1:	enzymatic activity, induced ( 2 ) , intracellular localization ( 2 , 4 , 5 ) , phosphorylation ( 2 ) , protein conformation ( 3 ) , ubiquitination ( 4 )
Effects of modification on biological processes:	autophagy, induced ( 2 )

References
1	Akabane S, et al. (2016) Constitutive Activation of PINK1 Protein Leads to Proteasome-mediated and Non-apoptotic Cell Death Independently of Mitochondrial Autophagy. J Biol Chem 291, 16162-74 27302064 Curated Info
2	Aerts L, Craessaerts K, De Strooper B, Morais VA (2015) PINK1 Kinase Catalytic Activity Is Regulated by Phosphorylation on Serines 228 and 402. J Biol Chem 290, 2798-811 25527497 Curated Info
3	Okatsu K, et al. (2013) A Dimeric PINK1-containing Complex on Depolarized Mitochondria Stimulates Parkin Recruitment. J Biol Chem 288, 36372-84 24189060 Curated Info
4	Iguchi M, et al. (2013) Parkin-catalyzed Ubiquitin-Ester Transfer Is Triggered by PINK1-dependent Phosphorylation. J Biol Chem 288, 22019-32 23754282 Curated Info
5	Okatsu K, et al. (2012) PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria. Nat Commun 3, 1016 22910362 Curated Info